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Structural differences of amyloid-β fibrils revealed by antibodies from phage display

Overview of attention for article published in BMC Biotechnology, June 2015
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • One of the highest-scoring outputs from this source (#9 of 460)
  • High Attention Score compared to outputs of the same age (92nd percentile)
  • High Attention Score compared to outputs of the same age and source (94th percentile)

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2 news outlets
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2 tweeters

Citations

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9 Dimensions

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44 Mendeley
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Title
Structural differences of amyloid-β fibrils revealed by antibodies from phage display
Published in
BMC Biotechnology, June 2015
DOI 10.1186/s12896-015-0146-8
Pubmed ID
Authors

Patrick Droste, André Frenzel, Miriam Steinwand, Thibaut Pelat, Philippe Thullier, Michael Hust, Hilal Lashuel, Stefan Dübel

Abstract

Beside neurofibrillary tangles, amyloid plaques are the major histological hallmarks of Alzheimer's disease (AD) being composed of aggregated fibrils of β-amyloid (Aβ). During the underlying fibrillogenic pathway, starting from a surplus of soluble Aβ and leading to mature fibrils, multiple conformations of this peptide appear, including oligomers of various shapes and sizes. To further investigate the fibrillization of β-amyloid and to have tools at hand to monitor the distribution of aggregates in the brain or even act as disease modulators, it is essential to develop highly sensitive antibodies that can discriminate between diverse aggregates of Aβ. Here we report the generation and characterization of a variety of amyloid-β specific human and human-like antibodies. Distinct fractions of monomers and oligomers of various sizes were separated by size exclusion chromatography (SEC) from Aβ42 peptides. These antigens were used for the generation of two Aβ42 specific immune scFv phage display libraries from macaque (Macaca fascicularis). Screening of these libraries as well as two naïve human phage display libraries resulted in multiple unique binders specific for amyloid-β. Three of the obtained antibodies target the N-terminal part of Aβ42 although with varying epitopes, while another scFv binds to the α-helical central region of the peptide. The affinities of the antibodies to various Aβ42 aggregates as well as their ability to interfere with fibril formation and disaggregation of preformed fibrils were determined. Most significantly, one of the scFv is fibril-specific and can discriminate between two different fibril forms resulting from variations in the acidity of the milieu during fibrillogenesis. We demonstrated that the approach of animal immunization and subsequent phage display based antibody selection is applicable to generate highly specific anti β-amyloid scFvs that are capable of accurately discriminating between minute conformational differences.

Twitter Demographics

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Mendeley readers

The data shown below were compiled from readership statistics for 44 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Greece 1 2%
France 1 2%
Germany 1 2%
Unknown 41 93%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 15 34%
Student > Master 9 20%
Researcher 5 11%
Student > Bachelor 3 7%
Student > Postgraduate 3 7%
Other 6 14%
Unknown 3 7%
Readers by discipline Count As %
Agricultural and Biological Sciences 15 34%
Biochemistry, Genetics and Molecular Biology 11 25%
Engineering 5 11%
Neuroscience 2 5%
Chemistry 2 5%
Other 6 14%
Unknown 3 7%

Attention Score in Context

This research output has an Altmetric Attention Score of 18. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 12 March 2016.
All research outputs
#404,790
of 7,382,271 outputs
Outputs from BMC Biotechnology
#9
of 460 outputs
Outputs of similar age
#17,716
of 223,597 outputs
Outputs of similar age from BMC Biotechnology
#2
of 37 outputs
Altmetric has tracked 7,382,271 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 94th percentile: it's in the top 10% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 460 research outputs from this source. They receive a mean Attention Score of 4.6. This one has done particularly well, scoring higher than 98% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 223,597 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 92% of its contemporaries.
We're also able to compare this research output to 37 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 94% of its contemporaries.